ID   FRZG_MYXXA              Reviewed;         334 AA.
AC   P31758;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Protein-glutamate methylesterase FrzG;
DE            EC=3.1.1.61;
GN   Name=frzG;
OS   Myxococcus xanthus.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=34;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=DZF1;
RX   PubMed=2168368; DOI=10.1128/jb.172.9.4877-4887.1990;
RA   McCleary W.R., McBride M.J., Zusman D.R.;
RT   "Developmental sensory transduction in Myxococcus xanthus involves
RT   methylation and demethylation of FrzCD.";
RL   J. Bacteriol. 172:4877-4887(1990).
CC   -!- FUNCTION: Probable methylesterase (By similarity). Required for the
CC       normal aggregation of M.xanthus cells during fruiting body formation.
CC       It is also a component of a sensory transduction pathway that controls
CC       the frequency at which cells reverse their gliding direction. It may
CC       remove the methyl group from the gamma-glutamyl methyl ester residues
CC       in FrzCD. {ECO:0000250, ECO:0000269|PubMed:2168368}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-
CC         glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, Rhea:RHEA-
CC         COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973,
CC         ChEBI:CHEBI:82795; EC=3.1.1.61;
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DR   EMBL; M35200; AAA25397.1; -; Genomic_DNA.
DR   PIR; A36707; A36707.
DR   RefSeq; WP_011554142.1; NZ_JABFNQ010000003.1.
DR   AlphaFoldDB; P31758; -.
DR   SMR; P31758; -.
DR   GeneID; 41361458; -.
DR   OMA; YGMPMAV; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   CDD; cd16432; CheB_Rec; 1.
DR   Gene3D; 3.40.50.180; -; 1.
DR   InterPro; IPR008248; CheB-like.
DR   InterPro; IPR035909; CheB_C.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   PIRSF; PIRSF000876; RR_chemtxs_CheB; 1.
DR   SUPFAM; SSF52738; SSF52738; 1.
DR   PROSITE; PS50122; CHEB; 1.
PE   3: Inferred from homology;
KW   Chemotaxis; Hydrolase.
FT   CHAIN           1..334
FT                   /note="Protein-glutamate methylesterase FrzG"
FT                   /id="PRO_0000158059"
FT   DOMAIN          147..334
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00050"
SQ   SEQUENCE   334 AA;  35497 MW;  3C0D924C5F2F8C93 CRC64;
     MAFRVLMVGK GLRALAARGL FDGESLVPVG PAEVDFAGAL VAVQRHFPDV VLVDLSALDA
     LPAIEHVMVE RPVPVLALHP GVLSGQEAFQ AMVAGALDVL ERPANPGPEF WTHVSRKLVL
     LAQVKAVRQV QTRPPPQAAR EAKPPPPYPL VAIAASLGGP KAVAQVLRMI PRAFPAPIAY
     CQHISDGFTE GLAHWLSNET ALRVLEAEHD VLMAPGTVYI APSGSHLLVR PEGRLELDAG
     PALRGFRPSC DMLLTSAGES FGPRCIGVIL TGMGRDGARG LKEIRERGGR TIAQDEASSV
     VWGMPREAVL MGAAHEVLPL SRIGAALMQW VDVC